Structure of PDB 5d3c Chain A

Receptor sequence

>5d3cA (length=159) Species: 9606 (Homo sapiens)

MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYAYVDINTFRLSADD
IRGIQSLYG

3D structure

• PDB: 5d3c Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played by the Zinc-Binding Group on Potency and Selectivity.
• Chain: A
• Resolution: 1.314 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H114 E115 H118 H124
• Enzyme Commision number: 3.4.24.65: macrophage elastase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H218 H222 H228	H114 H118 H124
BS02	ZN	A	H168 D170 H183 H196	H64 D66 H79 H92
BS03	CA	A	D158 G190 G192 D194	D54 G86 G88 D90
BS04	CA	A	D124 E199 E201	D20 E95 E97
BS05	CA	A	D175 G176 G178 I180 D198 E201	D71 G72 G74 I76 D94 E97
BS06	56O	A	G178 G179 I180 L181 A182 T215 H218 E219 H222 H228 K233 V235 P238 T239 Y240 F248	G74 G75 I76 L77 A78 T111 H114 E115 H118 H124 K129 V131 P134 T135 Y136 F144	PDBbind-CN: -logKd/Ki=10.40,Kd=40pM

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity
• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0031012 extracellular matrix

External links

• PDB: RCSB:5d3c, PDBe:5d3c, PDBj:5d3c
• PDBsum: 5d3c
• PubMed: 27996256
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)